Mobility and interactions of coronavirus nonstructural protein 4. - Wikidata - awgldk - TriplyDB

Mobility and interactions of coronavirus nonstructural protein 4.

Mobility and interactions of coronavirus nonstructural protein 4.

http://www.wikidata.org/entity/Q30501719

about

Coronavirus replicase-reporter fusions provide quantitative analysis of replication and replication complex formation.Mutations across murine hepatitis virus nsp4 alter virus fitness and membrane modifications.Coronavirus envelope (E) protein remains at the site of assembly Severe acute respiratory syndrome coronavirus nonstructural proteins 3, 4, and 6 induce double-membrane vesicles Murine hepatitis virus nsp4 N258T mutants are not temperature-sensitive.Untangling membrane rearrangement in the nidovirales.In Situ Tagged nsp15 Reveals Interactions with Coronavirus Replication/Transcription Complex-Associated Proteins.Biogenesis and dynamics of the coronavirus replicative structures.Involvement of autophagy in coronavirus replication.Illuminating the Sites of Enterovirus Replication in Living Cells by Using a Split-GFP-Tagged Viral Protein.Extensive coronavirus-induced membrane rearrangements are not a determinant of pathogenicity.Spherules and IBV.Expression and Cleavage of Middle East Respiratory Syndrome Coronavirus nsp3-4 Polyprotein Induce the Formation of Double-Membrane Vesicles That Mimic Those Associated with Coronaviral RNA Replication.Infectious Bronchitis Virus Nonstructural Protein 4 Alone Induces Membrane Pairing

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P2860

Mobility and interactions of coronavirus nonstructural protein 4.

http://www.wikidata.org/entity/Q30501719

description

2011 nî lūn-bûn

@nan

2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Mobility and interactions of coronavirus nonstructural protein 4.

@ast

Mobility and interactions of coronavirus nonstructural protein 4.

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type

label

Mobility and interactions of coronavirus nonstructural protein 4.

@ast

Mobility and interactions of coronavirus nonstructural protein 4.

@en

prefLabel

Mobility and interactions of coronavirus nonstructural protein 4.

@ast

Mobility and interactions of coronavirus nonstructural protein 4.

@en

P1433

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P1433

Journal of Virology

P1476

Mobility and interactions of coronavirus nonstructural protein 4.

@en

P2093

Annelotte M Vonk

http://www.w3.org/2001/XMLSchema#string

Cornelis A M de Haan

http://www.w3.org/2001/XMLSchema#string

Marne C Hagemeijer

http://www.w3.org/2001/XMLSchema#string

Mustafa Ulasli

http://www.w3.org/2001/XMLSchema#string

P2860

SARS-coronavirus replication is supported by a reticulovesicular network of modified endoplasmic reticulum

Assembly of the coronavirus envelope: homotypic interactions between the M proteins

The Coronavirus Spike Protein Is a Class I Virus Fusion Protein: Structural and Functional Characterization of the Fusion Core Complex

Localization and Membrane Topology of Coronavirus Nonstructural Protein 4: Involvement of the Early Secretory Pathway in Replication

Mouse Hepatitis Coronavirus RNA Replication Depends on GBF1-Mediated ARF1 Activation

Topology and Membrane Anchoring of the Coronavirus Replication Complex: Not All Hydrophobic Domains of nsp3 and nsp6 Are Membrane Spanning

Murine Hepatitis Virus Nonstructural Protein 4 Regulates Virus-Induced Membrane Modifications and Replication Complex Function

Dynamics of coronavirus replication-transcription complexes.

Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase

The coronavirus nucleocapsid protein is dynamically associated with the replication-transcription complexes.

P304

4572-4577

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scholarly article

P356

10.1128/JVI.00042-11

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P433

9

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P478

85

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Fulvio Reggiori

Peter J M Rottier

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2011-02-23T00:00:00Z

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P5875

49966674

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P698

21345958

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P921

molecular biology

Murine coronavirus inf-MHV-A59

P932

3126240

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